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Q79ZR7 (Q79ZR7_STRAW) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 38. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
3-oxoacyl-[acyl-carrier-protein] synthase 3 1 HAMAP MF_01815
EC=2.3.1.180 HAMAP MF_01815
Alternative name(s):
3-oxoacyl-[acyl-carrier-protein] synthase III 1 HAMAP MF_01815
Beta-ketoacyl-ACP synthase III 1 HAMAP MF_01815
Gene names
Name:fabH4 EMBL BAC68319.2
Synonyms:fabH1 HAMAP MF_01815
Ordered Locus Names:SAV_609 EMBL BAC68319.2
OrganismStreptomyces avermitilis [Complete proteome] [HAMAP]
Taxonomic identifier33903 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptomycineae › Streptomycetaceae › Streptomyces

Protein attributes

Sequence length331 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids By similarity. HAMAP MF_01815

Catalytic activity

Acetyl-CoA + malonyl-[acyl-carrier-protein] = acetoacetyl-[acyl-carrier-protein] + CoA + CO2. HAMAP MF_01815

Pathway

Lipid metabolism; fatty acid biosynthesis. HAMAP MF_01815 SAAS SAAS013747

Subunit structure

Homodimer By similarity. HAMAP MF_01815 SAAS SAAS013747

Subcellular location

Cytoplasm By similarity HAMAP MF_01815 SAAS SAAS013747.

Domain

The last Arg residue of the ACP-binding site is essential for the weak association between ACP/AcpP and FabH By similarity. HAMAP MF_01815

Sequence similarities

Belongs to the FabH family. HAMAP MF_01815

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region238 – 2425ACP-binding By similarity HAMAP MF_01815

Sites

Active site951 By similarity HAMAP MF_01815
Active site2371 By similarity HAMAP MF_01815
Active site2671 By similarity HAMAP MF_01815

Sequences

Sequence LengthMass (Da)Tools
Q79ZR7 [UniParc].

Last modified July 24, 2007. Version 1.
Checksum: 09E9231EA08EC043

FASTA33134,471
        10         20         30         40         50         60 
MVTNEHLARR LDTDDAWIRT RTGIRRRHAV DPGQATSDLA VEAGRRALVC AATASVDAVV 

        70         80         90        100        110        120 
VATTTPDHSC PATAPAVAAR LGLTGAAAFD ISAVCTGFVY GLASAAGLIA AGVAERVLLI 

       130        140        150        160        170        180 
GADTYSTIVD PLDRANAIIF GDGAGAVVLR AGHPDEPGAV GHFDLGSDGA HEDLIMVAAG 

       190        200        210        220        230        240 
GSRQRSRPGE PSRQDRHFGM RGKEVYRHAV TRMAESARAT LSRAGWKTDD VDHFVPHQAN 

       250        260        270        280        290        300 
LRILHSVADD LGLPRERCVT HVESVGNTGA ASIPLALADA AAGQTLRPGD RVLLTAFGGG 

       310        320        330 
LTWGSCLLTW PTLPAPAPPY DPHAQGERTT S

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References

[1]"Complete genome sequence and comparative analysis of the industrial microorganism Streptomyces avermitilis."
Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T., Sakaki Y., Hattori M., Omura S.
Nat. Biotechnol. 21:526-531(2003) [PubMed: 12692562] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]"Genome sequence of an industrial microorganism Streptomyces avermitilis: deducing the ability of producing secondary metabolites."
Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M., Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T., Sakaki Y., Hattori M.
Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001) [PubMed: 11572948] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BA000030 Genomic DNA. Translation: BAC68319.2.
RefSeqNP_821784.2. NC_003155.4.

3D structure databases

ProteinModelPortalQ79ZR7.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1210071.
GenomeReviewsGene locus SAV609 in contig BA000030_GR.
KEGGsma:SAV_609.
PATRIC23714492. VBIStrAve112782_0664.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG649927.
OMADYFILHQ.
ProtClustDBPRK09352.

Family and domain databases

HAMAPMF_01815. FabH.
[Tree]
InterProIPR013751. ACP_syn_III.
IPR013747. ACP_syn_III_C.
IPR004655. FabH_synth.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
[Graphical view]
Gene3DG3DSA:3.40.47.10. Thiolase-like_subgr. 2 hits.
KOK00648.
PfamPF08545. ACP_syn_III. 1 hit.
PF08541. ACP_syn_III_C. 1 hit.
[Graphical view]
SUPFAMSSF53901. Thiolase-like. 1 hit.
TIGRFAMsTIGR00747. FabH. 1 hit.
ProtoNetSearch...

Entry information

Entry nameQ79ZR7_STRAW
AccessionPrimary (citable) accession number: Q79ZR7
Entry history
Integrated into UniProtKB/TrEMBL: July 24, 2007
Last sequence update: July 24, 2007
Last modified: December 14, 2011
This is version 38 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info